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ProteomicsProteome-wide identification of SUMO2 modification sites
Posttranslational modification with small ubiquitin-like modifiers (SUMOs) alters the function of proteins involved in diverse cellular processes. SUMOs are conjugated to lysine residues in target proteins by SUMO-specific enzymes. Although proteomic studies have identified hundreds of sumoylated su...
ORGANISM(S): Homo sapiens (Human) 
2014-10-15 | PXD001281 | Pride
Heat-shock Sumo modification sites Hek293 
ProteomicsProteome-wide identification of SUMO2 modification sites
Posttranslational modification with small ubiquitin-like modifiers (SUMOs) alters the function of proteins involved in diverse cellular processes. SUMOs are conjugated to lysine residues in target proteins by SUMO-specific enzymes. Although proteomic studies have identified hundreds of sumoylated su...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080741 | MassIVE
ProteomicsComparison of LFQ and IPTL for protein identification and relative quantification
Mass spectrometry-based quantitative proteome profiling is most commonly performed by label-free quantification (LFQ), stable isotopic labeling with amino acids in cell culture (SILAC), and reporter-ion based isobaric labeling methods (TMT and iTRAQ). Isobaric peptide termini labeling (IPTL) was des...
ORGANISM(S): Homo sapiens (Human) 
2022-02-17 | PXD026942 | Pride
Tmt Silac Lfq Quantitative proteomics Iptl 
UnknownComparison of LFQ and IPTL for Protein Identification and Relative Quantification.
Not available
S-EPMC8433885 | biostudies-literature
UnknownProteome-wide identification of SUMO2 modification sites.
Not available
S-EPMC4051997 | biostudies-literature
ProteomicsLC-MS/MS of the reaction center-light harvesting 1 complex from Gemmatimonas phototrophica
Gemmatimonas phototrophica is the only phototrophic member of the recently discovered bacterial phylum Gemmatimonadetes. It was isolated from a freshwater lake in the Gobi desert and first described in 2014. So far, Gemmatimonas phototrophica is the only bacterium to have received a complete set of ...
ORGANISM(S): Gemmatimonas phototrophica 
2022-04-04 | PXD024609 | Pride
Lc-ms/ms Gemmatimonas phototrophica Reaction center light-harvesting-1 complex Photosynthesis Gemmatimonadetes 
ProteomicsSerine-Threonine Kinase Encoded by a Split hipA Homologous Gene of Escherichia coli Inhibits Tryptophanyl-tRNA Synthetase
Type II toxin – antitoxin modules encode a stable toxin that inhibits translation, replication or cell wall synthesis and an unstable protein antitoxin that neutralizes the toxin by direct protein – protein contact. The hipBA module of Escherichia coli K-12 codes for HipA, a eukaryote-like serine/th...
ORGANISM(S): Escherichia coli 
2019-06-24 | PXD012023 | Pride
E. coli Kinase Phosphorylation 
ProteomicsMethylated-antibody affinity purification to improve proteomic identification of plant RNA polymerase Pol V complex and the interacting proteins
Affinity purification followed by enzymatic digestion and mass spectrometry has been widely utilized for the sensitive detection of interacting proteins and protein complexes in various organisms. In plants, the method is technically challenging due to the low abundance proteins, non-specific bindin...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2017-02-28 | PXD005422 | Pride
On-bead digestion Pol v complex Chemical cross-link Reductive methylation Ap-ms 
UnknownClassification of microbial α-amylases for food manufacturing using proteinase digestion.
Not available
S-EPMC4237487 | biostudies-literature
ProteomicsShotgun proteomic analysis of pancreatic cancer cell lines vs. normal epithelial ductal pancreatic cells
We have run a shotgun proteomic analysis of cell lysates from pancreatic cancer cell lines (PANC-1, PaCa-44, MIA PaCa-2 and BxPC-3) vs. normal epithelial ductal pancreatic cells (HPDE) in LC-MS/MS. No labelling was performed and digestion was done with Trypsin/Lys-C mix endoproteinase.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-02-07 | MSV000084935 | MassIVE
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